Lipid modification of the 15 kiloDalton major membrane immunogen of Treponema pallidum.
The 15 kiloDalton major membrane immunogen was included among the Treponema pallidum polypeptides selectively labelled with [3H]-palmitate. The cloned gene for this immunogen, tpp15, encoded a signal peptide of 17 amino acids, a consensus signal peptidase II cleavage site, and a mature protein of 124 amino acids (13,967 Daltons). As predicted by the DNA sequence, the recombinant 15 kiloDalton immunogen labelled selectively with [3H]-palmitate, and globomycin inhibited processing of the precursor to the mature polypeptide. While the native and recombinant immunogens are amphiphilic, the 15 kiloDalton immunogen synthesized in a cell-free system was hydrophilic. The covalent attachment of fatty acids appears to be responsible for the amphiphilicity of the immunogen and its membrane attachment.
Purcell
B K
BK
Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas 75235.
Swancutt
M A
MA
Radolf
J D
JD
D000215:Acylation; D000595:Amino Acid Sequence; D000942:Antigens, Bacterial / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D001483:Base Sequence; D002474:Cell-Free System; D003001:Cloning, Molecular; D016384:Consensus Sequence; D005798:Genes, Bacterial; D015151:Immunoblotting; D050356:Lipid Metabolism; D008969:Molecular Sequence Data; D015183:Restriction Mapping; D014170:Transformation, Genetic; D014210:Treponema pallidum / Q000235:genetics / Q000276:immunology* / Q000378:metabolism
D000942:Antigens, Bacterial; C067191:major membrane immunogen, Treponema pallidum 15K